Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
48
pubmed:dateCreated
2000-12-18
pubmed:abstractText
ClpB is a member of a protein-disaggregating multi-chaperone system in Escherichia coli. The mechanism of protein-folding reactions mediated by ClpB is currently unknown, and the functional role of different sequence regions in ClpB is under discussion. We have expressed and purified the full-length ClpB and three truncated variants with the N-terminal, C-terminal, and a double N- and C-terminal deletion. We studied the protein concentration-dependent and ATP-induced oligomerization of ClpB, casein-induced activation of ClpB ATPase, and ClpB-assisted reactivation of denatured firefly luciferase. We found that both the N- and C-terminal truncation of ClpB strongly inhibited its chaperone activity. The reasons for such inhibition were different, however, for the N- and C-terminal truncation. Deletion of the C-terminal domain inhibited the self-association of ClpB, which led to decreased affinity for ATP and to decreased ATPase and chaperone activity of the C-terminally truncated variants. In contrast, deletion of the N-terminal domain did not inhibit the self-association of ClpB and its basal ATPase activity but decreased the ability of casein to activate ClpB ATPase. These results indicate that the N-terminal region of ClpB may contain a functionally significant protein-binding site, whereas the main role of the C-terminal region is to support oligomerization of ClpB.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/10982797-10359771, http://linkedlifedata.com/resource/pubmed/commentcorrection/10982797-10377389, http://linkedlifedata.com/resource/pubmed/commentcorrection/10982797-10485712, http://linkedlifedata.com/resource/pubmed/commentcorrection/10982797-10493591, http://linkedlifedata.com/resource/pubmed/commentcorrection/10982797-10497158, http://linkedlifedata.com/resource/pubmed/commentcorrection/10982797-10570141, http://linkedlifedata.com/resource/pubmed/commentcorrection/10982797-10583944, http://linkedlifedata.com/resource/pubmed/commentcorrection/10982797-10693812, http://linkedlifedata.com/resource/pubmed/commentcorrection/10982797-1122033, http://linkedlifedata.com/resource/pubmed/commentcorrection/10982797-1400361, http://linkedlifedata.com/resource/pubmed/commentcorrection/10982797-1416025, http://linkedlifedata.com/resource/pubmed/commentcorrection/10982797-1480111, http://linkedlifedata.com/resource/pubmed/commentcorrection/10982797-161695, http://linkedlifedata.com/resource/pubmed/commentcorrection/10982797-2066329, http://linkedlifedata.com/resource/pubmed/commentcorrection/10982797-8308017, http://linkedlifedata.com/resource/pubmed/commentcorrection/10982797-8376377, http://linkedlifedata.com/resource/pubmed/commentcorrection/10982797-8772382, http://linkedlifedata.com/resource/pubmed/commentcorrection/10982797-8977122, http://linkedlifedata.com/resource/pubmed/commentcorrection/10982797-9428517, http://linkedlifedata.com/resource/pubmed/commentcorrection/10982797-9601038, http://linkedlifedata.com/resource/pubmed/commentcorrection/10982797-9674429
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
275
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
37565-71
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Structure and activity of ClpB from Escherichia coli. Role of the amino-and -carboxyl-terminal domains.
pubmed:affiliation
Department of Biochemistry, Kansas State University, Manhattan, Kansas 66506, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.